Purification Propensity for Proteins from Bacillus halodurans


The demand for proteins with special purposes increases significantly. These proteins are generally obtained through recombinant proteins; however their purification is costly and not easy. It is necessarily important to develop a method to estimate the chance of purification beforehand in order to have a prospective on proteins in question. Purification of a protein should be related to instinct properties of a protein including its 3D structure, and so far around 540 amino acid properties are found.

Thus it is possible to test each amino acid property against the successful rate of protein purification to find out which property is more suitable to estimate the purification propensity. In this study, each of 535 properties was tested against 438 purified and 429 impossible purified proteins from Bacillus halodurans using logistic regression and neural network model. ROC analysis was applied to the resultant sensitivity and specificity.

The results show that amino acid composition properties were generally less helpful to estimate the purification propensity whereas amino acid physicochemical properties, secondary structures and dynamic properties were more useful, and dynamic properties were more promising. Therefore several types of protein properties can serve to determine purification propensity of proteins, and have the potential to reduce the cost and to speed up the production in microbiological and biotechnical fields.

The demand for proteins with special purposes increases significantly, for example, special proteins are in good need in development of sensitive, specific and reliable differential diagnostic assays. To meet such huge demand, proteins of interest can be expressed in either prokaryotic or eukaryotic cells, like Escherichia coli, to produce recombinant proteins. However, this is not an easy task and is often costly. Purification of recombinant proteins from plant biomass currently accounts for almost 80% of production cost.

In order to develop an efficient and cost-effective purification scheme, many efforts have been made and much has been achieved in finding the factors that affect protein purification. At codon optimization level, N-terminal rare codons increase expression with some reservation. At protein terminal level, hydrophilicity of histidine tag enhances the high solubility of expressed recombinant fusion proteins. At protein level, polyhedrin is used as a carrier protein to facilitate antigen purification.

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